Partial functional replacement of CymA by SirCD in Shewanella oneidensis MR-1.

TitlePartial functional replacement of CymA by SirCD in Shewanella oneidensis MR-1.
Publication TypeJournal Article
Year of Publication2011
AuthorsCordova, CD, Schicklberger MFR, Yu Y, Spormann AM
JournalJournal of bacteriology
Date Published2011 May
KeywordsBacterial Proteins, Base Sequence, Conserved Sequence, DNA Transposable Elements, Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Genome, Bacterial, Mutation, Oxidoreductases, Shewanella
AbstractThe gammaproteobacterium Shewanella oneidensis MR-1 utilizes a complex electron transfer network composed primarily of c-type cytochromes to respire under anoxic conditions a variety of compounds, including fumarate, nitrate, and dimethyl sulfoxide (DMSO), in addition to the minerals Fe(III) and Mn(IV). Central to several respiratory pathways is CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome that functions as the major hydroquinone dehydrogenase. To investigate functional redundancy and plasticity in S. oneidensis MR-1 electron transport, we isolated ΔcymA suppressor mutants and characterized one biochemically and genetically. Interestingly, in the characterized ΔcymA suppressor mutant, respiration of fumarate, ferric citrate, and DMSO was restored but that of nitrate was not. The suppression was found to be due to transcriptional activation of sirC and sirD, encoding a periplasmic iron sulfur protein and an integral membrane hydroquinone dehydrogenase, respectively. Biochemical in vitro reconstitution experiments confirmed electron transport between formate and fumarate via fumarate reductase by suppressor membrane fractions. The suppression was found to be caused by insertion of an ISSod1 element upstream of the sirCD transcriptional start site, generating a novel, constitutively active hybrid promoter. This work revealed that adaptation of an alternative electron transfer pathway from quinol to terminal oxidoreductases independent of CymA occurs rapidly in S. oneidensis MR-1.
Alternate JournalJ. Bacteriol.
0 August 12, 2011